scholarly journals Correction: Analysis of long dsRNA produced in vitro and in vivo using atomic force microscopy in conjunction with ion-pair reverse-phase HPLC

The Analyst ◽  
2019 ◽  
Vol 144 (22) ◽  
pp. 6773-6773
Author(s):  
Alison O. Nwokeoji ◽  
Sandip Kumar ◽  
Peter M. Kilby ◽  
David E. Portwood ◽  
Jamie K. Hobbs ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Ion Pair ◽  
Reverse Phase Hplc ◽  
Reverse Phase ◽  
Force Microscopy ◽  
Atomic Force

Correction for ‘Analysis of long dsRNA produced in vitro and in vivo using atomic force microscopy in conjunction with ion-pair reverse-phase HPLC’ by Alison O. Nwokeoji, et al., Analyst, 2019, 144, 4985–4994.

scholarly journals Analysis of long dsRNA produced in vitro and in vivo using atomic force microscopy in conjunction with ion-pair reverse-phase HPLC

The Analyst ◽  
2019 ◽  
Vol 144 (16) ◽  
pp. 4985-4994
Author(s):  
Alison O. Nwokeoji ◽  
Sandip Kumar ◽  
Peter M. Kilby ◽  
David E. Portwood ◽  
Jamie K. Hobbs ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
High Performance ◽  
Ion Pair ◽  
Reverse Phase Hplc ◽  
Reverse Phase ◽  
Force Microscopy ◽  
Atomic Force ◽  
Insight Into

Atomic force microscopy (AFM) in conjunction with ion-pair reverse-phase high performance liquid chromatography (IP-RP-HPLC) provides novel insight into dsRNA for RNAi applications.

scholarly journals Computational model for nanocarrier binding to endothelium validated using in vivo, in vitro, and atomic force microscopy experiments

2010 ◽  
Vol 107 (38) ◽  
pp. 16530-16535 ◽  
Author(s):  
J. Liu ◽  
G. E. R. Weller ◽  
B. Zern ◽  
P. S. Ayyaswamy ◽  
D. M. Eckmann ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Computational Model ◽  
Force Microscopy ◽  
Atomic Force

MORPHOLOGY OF ADSORBED COLLAGEN LAYERS OBSERVED BY ATOMIC FORCE MICROSCOPY

2009 ◽  
Vol 21 (05) ◽  
pp. 311-316
Author(s):  
Yih-Pey Yang ◽  
Chia-Chi Lin
Keyword(s):  
Atomic Force Microscopy ◽  
Type I Collagen ◽  
Fibrillar Structure ◽  
Collagen Molecule ◽  
Nanometer Scale ◽  
Type I ◽  
Force Microscopy ◽  
Atomic Force

The interaction between cells and biomaterials strongly depends on the assembled structure of collagen adsorption upon the solid surface. Due to its self-assembling property, Type I collagen may aggregate and form fibrils in vivo and in vitro. This study utilizes an atomic force microscope to investigate nanometer-scale organization of adsorbed Type I collagen layers on mica and on poly(methyl methacrylate) (PMMA). We have observed various film morphologies, depending on substrate hydrophobicity and the state of collagen solution used. On mica, the atomic force microscopy (AFM) study obtains dense felt-like structures of randomly distributed assemblies. Images of network-like assemblies composed of interwoven fibrils appear on PMMA. According to the above results, we believe that these assemblies are associated at the interface rather than aggregated in the solution. This work also investigates the adsorbed collagen structure on PMMA after collagen aggregation in solution, to realize the relation between adsorption and aggregation. Consequently, the result exhibits a dendritic fibrillar structure adsorbed on PMMA, following collagen molecule aggregation, to form a fibrillar structure in the solution. This result suggests that the adsorption of aggregates preformed in the solution is preferable to collagen molecules adsorption. This research created all assembled structures of adsorbed collagen layers in nanometer-scale thickness.

Rapid, Refined, and Robust Method for Expression, Purification, and Characterization of Recombinant Human Amyloid-beta M1-42

2019 ◽  
Author(s):  
Priya Prakash ◽  
Travis Lantz ◽  
Krupal P. Jethava ◽  
Gaurav Chopra
Keyword(s):  
Amyloid Beta ◽  
Western Blots ◽  
Force Microscopy ◽  
E Coli ◽  
Atomic Force ◽  
Set Up ◽  
Short Time

Amyloid plaques found in the brains of Alzheimer’s disease (AD) patients primarily consists of amyloid beta 1-42 (Ab42). Commercially, Ab42 is synthetized using peptide synthesizers. We describe a robust methodology for expression of recombinant human Ab(M1-42) in Rosetta(DE3)pLysS and BL21(DE3)pLysS competent E. coli with refined and rapid analytical purification techniques. The peptide is isolated and purified from the transformed cells using an optimized set-up for reverse-phase HPLC protocol, using commonly available C18 columns, yielding high amounts of peptide (~15-20 mg per 1 L culture) in a short time. The recombinant Ab(M1-42) forms characteristic aggregates similar to synthetic Ab42 aggregates as verified by western blots and atomic force microscopy to warrant future biological use. Our rapid, refined, and robust technique to purify human Ab(M1-42) can be used to synthesize chemical probes for several downstream in vitro and in vivo assays to facilitate AD research.

Diabetes increases stiffness of live cardiomyocytes measured by atomic force microscopy nanoindentation

2014 ◽  
Vol 307 (10) ◽  
pp. C910-C919 ◽  
Author(s):  
Juan C. Benech ◽  
Nicolás Benech ◽  
Ana I. Zambrana ◽  
Inés Rauschert ◽  
Verónica Bervejillo ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Physiological Condition ◽  
Diabetic Mice ◽  
Cell Nuclei ◽  
Buffer Solution ◽  
Isolated Cardiomyocytes ◽  
Force Microscopy ◽  
Atomic Force ◽  
Myocardial Fibers

Stiffness of live cardiomyocytes isolated from control and diabetic mice was measured using the atomic force microscopy nanoindentation method. Type 1 diabetes was induced in mice by streptozotocin administration. Histological images of myocardium from mice that were diabetic for 3 mo showed disorderly lineup of myocardial cells, irregularly sized cell nuclei, and fragmented and disordered myocardial fibers with interstitial collagen accumulation. Phalloidin-stained cardiomyocytes isolated from diabetic mice showed altered (i.e., more irregular and diffuse) actin filament organization compared with cardiomyocytes from control mice. Sarco/endoplasmic reticulum Ca2+-ATPase (SERCA2a) pump expression was reduced in homogenates obtained from the left ventricle of diabetic animals compared with age-matched controls. The apparent elastic modulus (AEM) for live control or diabetic isolated cardiomyocytes was measured using the atomic force microscopy nanoindentation method in Tyrode buffer solution containing 1.8 mM Ca2+ and 5.4 mM KCl (physiological condition), 100 nM Ca2+ and 5.4 mM KCl (low extracellular Ca2+ condition), or 1.8 mM Ca2+ and 140 mM KCl (contraction condition). In the physiological condition, the mean AEM was 112% higher for live diabetic than control isolated cardiomyocytes (91 ± 14 vs. 43 ± 7 kPa). The AEM was also significantly higher in diabetic than control cardiomyocytes in the low extracellular Ca2+ and contraction conditions. These findings suggest that the material properties of live cardiomyocytes were affected by diabetes, resulting in stiffer cells, which very likely contribute to high diastolic LV stiffness, which has been observed in vivo in some diabetes mellitus patients.

scholarly journals Visualization by atomic force microscopy of tobacco mosaic virus movement protein–RNA complexes formed in vitro

2001 ◽  
Vol 82 (6) ◽  
pp. 1503-1508 ◽  
Author(s):  
O. I. Kiselyova ◽  
I. V. Yaminsky ◽  
E. M. Karger ◽  
O. Yu. Frolova ◽  
Y. L. Dorokhov ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Structural Conversion ◽  
Force Microscopy ◽  
Rna Transcripts ◽  
Atomic Force ◽  
Rna Complexes

The structure of complexes formed in vitro by tobacco mosaic virus (TMV)-coded movement protein (MP) with TMV RNA and short (890 nt) synthetic RNA transcripts was visualized by atomic force microscopy on a mica surface. MP molecules were found to be distributed along the chain of RNA and the structure of MP–RNA complexes depended on the molar MP:RNA ratios at which the complexes were formed. A rise in the molar MP:TMV RNA ratio from 20:1 to 60–100:1 resulted in an increase in the density of the MP packaging on TMV RNA and structural conversion of complexes from RNase-sensitive ‘beads-on-a-string’ into a ‘thick string’ form that was partly resistant to RNase. The ‘thick string’-type RNase-resistant complexes were also produced by short synthetic RNA transcripts at different MP:RNA ratios. The ‘thick string’ complexes are suggested to represent clusters of MP molecules cooperatively bound to discrete regions of TMV RNA and separated by protein-free RNA segments.

scholarly journals In vivo dynamics of the cortical actin network revealed by fast-scanning atomic force microscopy

Microscopy ◽  
2017 ◽  
Vol 66 (4) ◽  
pp. 272-282 ◽  
Author(s):  
Yanshu Zhang ◽  
Aiko Yoshida ◽  
Nobuaki Sakai ◽  
Yoshitsugu Uekusa ◽  
Masahiro Kumeta ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Actin Network ◽  
Cortical Actin ◽  
Force Microscopy ◽  
Atomic Force
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